Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus

Nevin Gül-Karagüler; Richard B. Sessions; J. John Holbrook

doi:10.1023/A:1005687723905

Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus

Nevin Gül-Karagüler^*
, Richard B. Sessions
, J. John Holbrook

^*Bu çalışma için yazışmadan sorumlu yazar

Mol.Biyoloji ve Genetik Bölümü

University Walk

Araştırma sonucu: Dergiye katkı › Makale › bilirkişi

3 Atıf (Scopus)

Özet

A single residue of the NAD(H)-dependent lactate dehydrogenase (LDH) from Bacillus stearothermophilus has been changed in order to decrease substrate inhibition. The conserved aspartic acid residue at position 52 was replaced by glutamate using site-directed mutagenesis. The effect on substrate inhibition was measured. In the glutamate-52 mutant substrate inhibition is decreased twofold.

Orijinal dil	İngilizce
Sayfa (başlangıç-bitiş)	395-399
Sayfa sayısı	5
Dergi	Biotechnology Letters
Hacim	23
Basın numarası	5
DOI'lar	https://doi.org/10.1023/A:1005687723905
Yayın durumu	Yayınlandı - 2001

Belgeye Erişim

10.1023/A:1005687723905

Diğer Dosyalar ve Linkler

Link to publication in Scopus

Alıntı Yap

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title = "Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus",

abstract = "A single residue of the NAD(H)-dependent lactate dehydrogenase (LDH) from Bacillus stearothermophilus has been changed in order to decrease substrate inhibition. The conserved aspartic acid residue at position 52 was replaced by glutamate using site-directed mutagenesis. The effect on substrate inhibition was measured. In the glutamate-52 mutant substrate inhibition is decreased twofold.",

keywords = "Lactate dehydrogenase, Site-directed mutagenesis, Substrate inhibition",

author = "Nevin G{\"u}l-Karag{\"u}ler and Sessions, \{Richard B.\} and Holbrook, \{J. John\}",

year = "2001",

doi = "10.1023/A:1005687723905",

language = "English",

volume = "23",

pages = "395--399",

journal = "Biotechnology Letters",

issn = "0141-5492",

publisher = "Springer Science and Business Media B.V.",

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TY - JOUR

T1 - Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus

AU - Gül-Karagüler, Nevin

AU - Sessions, Richard B.

AU - Holbrook, J. John

PY - 2001

Y1 - 2001

N2 - A single residue of the NAD(H)-dependent lactate dehydrogenase (LDH) from Bacillus stearothermophilus has been changed in order to decrease substrate inhibition. The conserved aspartic acid residue at position 52 was replaced by glutamate using site-directed mutagenesis. The effect on substrate inhibition was measured. In the glutamate-52 mutant substrate inhibition is decreased twofold.

AB - A single residue of the NAD(H)-dependent lactate dehydrogenase (LDH) from Bacillus stearothermophilus has been changed in order to decrease substrate inhibition. The conserved aspartic acid residue at position 52 was replaced by glutamate using site-directed mutagenesis. The effect on substrate inhibition was measured. In the glutamate-52 mutant substrate inhibition is decreased twofold.

KW - Lactate dehydrogenase

KW - Site-directed mutagenesis

KW - Substrate inhibition

UR - https://www.scopus.com/pages/publications/0035120153

U2 - 10.1023/A:1005687723905

DO - 10.1023/A:1005687723905

M3 - Article

AN - SCOPUS:0035120153

SN - 0141-5492

VL - 23

SP - 395

EP - 399

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 5

ER -

Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus

Özet

Belgeye Erişim

Diğer Dosyalar ve Linkler

Parmak izi

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